KEGG ENZYME: 1.13.11.47

ENZYME: 1.13.11.47

Entry

EC 1.13.11.47               Enzyme

Name

3-hydroxy-4-oxoquinoline 2,4-dioxygenase;
(1H)-3-hydroxy-4-oxoquinoline 2,4-dioxygenase;
3-hydroxy-4-oxo-1,4-dihydroquinoline 2,4-dioxygenase;
3-hydroxy-4(1H)-one, 2,4-dioxygenase;
quinoline-3,4-diol 2,4-dioxygenase

Class

Oxidoreductases;
Acting on single donors with incorporation of molecular oxygen (oxygenases);
With incorporation of two atoms of oxygen

Sysname

3-hydroxy-1H-quinolin-4-one 2,4-dioxygenase (CO-forming)

Reaction(IUBMB)

3-hydroxy-1H-quinolin-4-one + O2 = N-formylanthranilate + CO [RN:R05719]

Reaction(KEGG)

R05719;
(other) R04915

Substrate

3-hydroxy-1H-quinolin-4-one [CPD:C11503];
O2 [CPD:C00007]

Product

N-formylanthranilate [CPD:C05653];
CO [CPD:C00237]

Comment

Does not contain a metal centre or organic cofactor. Fission of two C-C bonds: 2,4-dioxygenolytic cleavage with concomitant release of carbon monoxide. The enzyme from Pseudomonas putida is highly specific for this substrate.

History

EC 1.13.11.47 created 1999 as EC 1.13.99.5, transferred 2001 to EC 1.13.11.47 (EC 1.12.99.5 created 1999 deleted 2001 as identical)

Orthology

K20209

3-hydroxy-4-oxoquinoline 2,4-dioxygenase

Reference

Authors

Bauer, I., De Beyer, A., Tsisuaka, B., Fetzner, S. and Lingens, F.

Title

A novel type of oxygenolytic ring cleavage: 2,4-Oxygenation and decarbonylation of 1H-3-hydroxy-4-oxoquinaldine and 1H-3-hydroxy-4-oxoquinoline.

Journal

FEMS Microbiol Lett 117:299-304 (1994)

Reference

2 [PMID:8856057]

Authors

Bauer I, Max N, Fetzner S, Lingens F.

Title

2,4-dioxygenases catalyzing N-heterocyclic-ring cleavage and formation of carbon monoxide. Purification and some properties of 1H-3-hydroxy-4-oxoquinaldine 2,4-dioxygenase from Arthrobacter sp. Ru61a and comparison with 1H-3-hydroxy-4-oxoquinoline 2,4-dioxygenase from Pseudomonas putida 33/1.

Journal

Eur J Biochem 240:576-83 (1996)
DOI:10.1111/j.1432-1033.1996.0576h.x

Reference

3 [PMID:10482514]

Authors

Fischer F, Kunne S, Fetzner S

Title

Bacterial 2,4-dioxygenases: new members of the alpha/beta hydrolase-fold superfamily of enzymes functionally related to serine hydrolases.

Journal

J Bacteriol 181:5725-33 (1999)
DOI:10.1128/JB.181.18.5725-5733.1999

Sequence

[ag:CAA75082]